Research interest

Protein misfolding and aggregation are a well-known cause of several neurodegenerative disorders such as Alzheimer's disease , Parkinson's disease, prion disease etc.Although enormous efforts have been employed to ward off such diseases, the lack of our understanding of the mechanism of amyloid formation, its structural plasticity, polymorphism, and kinetic behavior restricts current therapeutic progress. In particular, the molecular mechanisms of structural conversion from a soluble protein to insoluble amyloids have remained elusive. Thus, I am interested in studying the mechanistic and structural basis of amyloid polymorphism (amyloid beta peptides) in the membrane system. I will integrate a variety of biophysical methods including NMR and ITC with MD simulation, and aim to “chase” the dynamic structural changes at the atomic resolution during seeding reaction ( amyloid formation ) in membrane system. The research findings and the high-resolution structure elucidation will be greatly helpful to develop therapeutic strategies for a variety of devastating neurodegenerative diseases in which amyloids are involved.